4ZM0

Antitoxin Phd from phage P1 in complex with its operator DNA inverted repeat

4ZM0 の概要

• エントリーDOI: 10.2210/pdb4zm0/pdb
• 関連するPDBエントリー: 4ZLX
• 分子名称: Antitoxin phd, DNA/RNA (5'-D(CP*TP*TP*GP*TP*GP*TP*AP*CP*AP*CP*AP*T)-3'), DNA/RNA (5'-D(CP*AP*TP*GP*TP*GP*TP*AP*CP*AP*CP*AP*A)-3'), ... (5 entities in total)
• 機能のキーワード: transcription factor, toxin-antitoxin, dna binding, intrinsic disorder, conditional cooperativity, protein-dna complex, transcription
• 由来する生物種: Enterobacteria phage P1; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 49958.79

構造登録者

Garcia-Pino, A.,Loris, R. (登録日: 2015-05-02, 公開日: 2016-04-20, 最終更新日: 2024-01-10)

主引用文献

Garcia-Pino, A.,De Gieter, S.,Talavera, A.,De Greve, H.,Efremov, R.G.,Loris, R.
An intrinsically disordered entropic switch determines allostery in Phd-Doc regulation.
Nat.Chem.Biol., 12:490-496, 2016

PubMed Abstract: Conditional cooperativity is a common mechanism involved in transcriptional regulation of prokaryotic type II toxin-antitoxin operons and is intricately related to bacterial persistence. It allows the toxin component of a toxin-antitoxin module to act as a co-repressor at low doses of toxin as compared to antitoxin. When toxin level exceeds a certain threshold, however, the toxin becomes a de-repressor. Most antitoxins contain an intrinsically disordered region (IDR) that typically is involved in toxin neutralization and repressor complex formation. To address how the antitoxin IDR is involved in transcription regulation, we studied the phd-doc operon from bacteriophage P1. We provide evidence that the IDR of Phd provides an entropic barrier precluding full operon repression in the absence of Doc. Binding of Doc results in a cooperativity switch and consequent strong operon repression, enabling context-specific modulation of the regulatory process. Variations of this theme are likely to be a common mechanism in the autoregulation of bacterial operons that involve intrinsically disordered regions.

PubMed: 27159580
DOI: 10.1038/nchembio.2078

実験手法

X-RAY DIFFRACTION (3.17 Å)